Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding.

@article{Bonmatin1992Twodimensional1N,
  title={Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding.},
  author={J. M. Bonmatin and J L Bonnat and Xavier Gallet and Françoise Vovelle and M. Ptak and J M Reichhart and James A. Hoffmann and E. Keppi and Mich{\`e}le Legrain and T. Achstetter},
  journal={Journal of biomolecular NMR},
  year={1992},
  volume={2 3},
  pages={235-56}
}
A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of… CONTINUE READING

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